APPBP1/6xHis-UBA3

APPBP1/UBA3 is the heterodimeric E1 enzyme that conjugates Nedd8 to protein substrates. Nedd8 is conjugated onto the catalytic cysteine residue of UBA3 by formation of a thioester bond in an ATP-dependent reaction. The activated Nedd8 is then passed on to an E2 (Ubc12) to be finally attached to a substrate. Nedd8 is mainly conjugated on Cullins to increase the activity of the Cullin – RING E3 Ub ligases.

Additional Information

Product Name: APPBP1/6xHis-UBA3
Also Known As: APPBP1 (NAE1;HPP1; ula-1; A-116A10.1); UBA3 (UBE1C; hUBA3; MGC22384; DKFZp566J164)
Catalog No.: B1401
Size: 100 µg
Molecular Weight: APPBP1 (60.2 kDa), UBA (51.8 kDa)
Species: Human
Source: Bacterial recombinant
Stock: 20 mM Tris, 150 mM NaCl, 2 mM βME, 10% Glycerol
Concentration: See tube label
Quality Assurance: ~95% by SDS-PAGE, see datasheet for gel image
Storage: Store at -80°C; avoid multiple freeze-thaw cycles
PDF Data Sheet: PDF DatasheetMSDS
NCBI RefSeq: NM_003905 (APPBP1); NM_003968 (UBA3)
Image(s): (Click image to enlarge)

Coomassie-stained SDS-PAGE
Lane 1: Molecular weight markers
Lane 2: 5 µg purified APPBP1/6xHis-UBA3
Shipping Method: Dry ice shipping
References: 1. Whitby FG, et al. (1998) J Biol Chem 273(52), 34983 – 34991.
2. Osaka F, et al. (1998) Genes Dev 12(15), 2263 – 2268.
3. Walden H, et al. (2003) Mol Cell 12(6), 1427 – 1437.
4. Schulman BA, et al. (2009) Nat Rev Mol Biol 10(5), 319 – 331.

Details

APPBP1/UBA3 is the heterodimeric E1 enzyme that conjugates Nedd8 to protein substrates. Nedd8 is conjugated onto the catalytic cysteine residue of UBA3 by formation of a thioester bond in an ATP-dependent reaction. The activated Nedd8 is then passed on to an E2 (Ubc12) to be finally attached to a substrate. Nedd8 is mainly conjugated on Cullins to increase the activity of the Cullin – RING E3 Ub ligases.

Images:
(Click image to enlarge)

Coomassie-stained SDS-PAGE
Lane 1: Molecular weight markers
Lane 2: 5 µg purified APPBP1/6xHis-UBA3